1zue

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(New page: 200px<br /><applet load="1zue" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zue" /> '''Revised Solution Structure of DLP-2'''<br />...)
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'''Revised Solution Structure of DLP-2'''<br />
'''Revised Solution Structure of DLP-2'''<br />
==Overview==
==Overview==
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The recent discovery that the natriuretic peptide OvCNPb (Ornithorhynchus, venom C-type natriuretic peptide B) from platypus (Ornithorynchus, anatinus) venom contains a D-amino acid residue suggested that other, D-amino-acid-containing peptides might be present in the venom. In the, present study, we show that DLP-2 (defensin-like peptide-2), a, 42-amino-acid residue polypeptide in the platypus venom, also contains a, D-amino acid residue, D-methionine, at position 2, while DLP-4, which has, an identical amino acid sequence, has all amino acids in the L-form. These, findings were supported further by the detection of isomerase activity in, the platypus gland venom extract that converts DLP-4 into DLP-2. In the, light of this new information, the tertiary structure of DLP-2 was, recalculated using a new structural template with D-Met2. The structure of, DLP-4 was also determined in order to evaluate the effect of a D-amino, acid at position 2 on the structure and possibly to explain the large, retention time difference observed for the two molecules in reverse-phase, HPLC. The solution structures of the DLP-2 and DLP-4 are very similar to, each other and to the earlier reported structure of DLP-2, which assumed, that all amino acids were in the L-form. Our results suggest that the, incorporation of the D-amino acid at position 2 has minimal effect on the, overall fold in solution.
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The recent discovery that the natriuretic peptide OvCNPb (Ornithorhynchus venom C-type natriuretic peptide B) from platypus (Ornithorynchus anatinus) venom contains a D-amino acid residue suggested that other D-amino-acid-containing peptides might be present in the venom. In the present study, we show that DLP-2 (defensin-like peptide-2), a 42-amino-acid residue polypeptide in the platypus venom, also contains a D-amino acid residue, D-methionine, at position 2, while DLP-4, which has an identical amino acid sequence, has all amino acids in the L-form. These findings were supported further by the detection of isomerase activity in the platypus gland venom extract that converts DLP-4 into DLP-2. In the light of this new information, the tertiary structure of DLP-2 was recalculated using a new structural template with D-Met2. The structure of DLP-4 was also determined in order to evaluate the effect of a D-amino acid at position 2 on the structure and possibly to explain the large retention time difference observed for the two molecules in reverse-phase HPLC. The solution structures of the DLP-2 and DLP-4 are very similar to each other and to the earlier reported structure of DLP-2, which assumed that all amino acids were in the L-form. Our results suggest that the incorporation of the D-amino acid at position 2 has minimal effect on the overall fold in solution.
==About this Structure==
==About this Structure==
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1ZUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZUE OCA].
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1ZUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUE OCA].
==Reference==
==Reference==
D-amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties., Torres AM, Tsampazi C, Geraghty DP, Bansal PS, Alewood PF, Kuchel PW, Biochem J. 2005 Oct 15;391(Pt 2):215-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16033333 16033333]
D-amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties., Torres AM, Tsampazi C, Geraghty DP, Bansal PS, Alewood PF, Kuchel PW, Biochem J. 2005 Oct 15;391(Pt 2):215-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16033333 16033333]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Alewood, P.F.]]
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[[Category: Alewood, P F.]]
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[[Category: Bansal, P.S.]]
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[[Category: Bansal, P S.]]
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[[Category: Geraghty, D.P.]]
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[[Category: Geraghty, D P.]]
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[[Category: Kuchel, P.W.]]
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[[Category: Kuchel, P W.]]
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[[Category: Torres, A.M.]]
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[[Category: Torres, A M.]]
[[Category: Tsampazi, C.]]
[[Category: Tsampazi, C.]]
[[Category: antiparallel beta-sheet]]
[[Category: antiparallel beta-sheet]]
[[Category: helix]]
[[Category: helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:40:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:12 2008''

Revision as of 14:19, 21 February 2008


1zue

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Revised Solution Structure of DLP-2

Overview

The recent discovery that the natriuretic peptide OvCNPb (Ornithorhynchus venom C-type natriuretic peptide B) from platypus (Ornithorynchus anatinus) venom contains a D-amino acid residue suggested that other D-amino-acid-containing peptides might be present in the venom. In the present study, we show that DLP-2 (defensin-like peptide-2), a 42-amino-acid residue polypeptide in the platypus venom, also contains a D-amino acid residue, D-methionine, at position 2, while DLP-4, which has an identical amino acid sequence, has all amino acids in the L-form. These findings were supported further by the detection of isomerase activity in the platypus gland venom extract that converts DLP-4 into DLP-2. In the light of this new information, the tertiary structure of DLP-2 was recalculated using a new structural template with D-Met2. The structure of DLP-4 was also determined in order to evaluate the effect of a D-amino acid at position 2 on the structure and possibly to explain the large retention time difference observed for the two molecules in reverse-phase HPLC. The solution structures of the DLP-2 and DLP-4 are very similar to each other and to the earlier reported structure of DLP-2, which assumed that all amino acids were in the L-form. Our results suggest that the incorporation of the D-amino acid at position 2 has minimal effect on the overall fold in solution.

About this Structure

1ZUE is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

D-amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties., Torres AM, Tsampazi C, Geraghty DP, Bansal PS, Alewood PF, Kuchel PW, Biochem J. 2005 Oct 15;391(Pt 2):215-20. PMID:16033333

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